OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 212 YSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQAL 291
Cdd:cd22796    1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334184505 292 AEMYNRPIHIYSYST-EPINIFQGNYSTDTPPIRLSYHHGNHYNSLVD 338
Cdd:cd22796   81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 212 YSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQAL 291
Cdd:cd22796    1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334184505 292 AEMYNRPIHIYSYST-EPINIFQGNYSTDTPPIRLSYHHGNHYNSLVD 338
Cdd:cd22796   81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 212 YSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQAL 291
Cdd:cd22796    1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334184505 292 AEMYNRPIHIYSYST-EPINIFQGNYSTDTPPIRLSYHHGNHYNSLVD 338
Cdd:cd22796   81 SEIYNRPIEVYSYSNgEPINIFHGSYEGDDPPIRLSYHDGNHYNSIID 128

OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 215 GFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEG--FTSYLKRKRRDKVYGNNVEIQALA 292
Cdd:cd22771    1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDDetFEDYVSRMREDGTWGGNLELQAAS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 334184505 293 EMYNRPIHIYSySTEPINIFQGNYSTDTPPIRLSYHHGNHYNS 335
Cdd:cd22771   81 LVYRVNIVVHQ-LGQPRWEIENFPDKGARTIHLSYHDGEHYNS 122

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 214 KGFEIRRMLEDGNCLFRAVADQV-----YGDSEAYDLARQMCMDYMEQERDHFSQFIT---------EGFTSYLKRKRRD 279
Cdd:cd22748    4 LGLRIKEIPPDGHCLYRAIADQLklrggSEEPYSYKELRKLAADYMRAHRDDFLPFLTnddgdlmteEEFEEYCDKIENT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334184505 280 KVYGNNVEIQALAEMYNRPIHIYSYSTEPINIfqGNYSTDTPPIRLSYHH-----GNHYNSLV 337
Cdd:cd22748   84 AEWGGQLELRALSKALKRPIHVYQAGSPPLVI--GEEFDSGEPLRLSYHRhayglGEHYNSVV 144

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 213 SKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLA--RQMCMDYMEQERDHF------SQFITEGFTSYLKRKRRDKVYGN 284
Cdd:cd22758    3 ENGFEIRDVPGDGNCFFHAVSDQLYGNGIEHSHKelRQQAVNYLRENPELYdgfflsEFDEEESWEEYLNRMSKDGTWGD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334184505 285 NVEIQALAEMYNRPIHIY-SYSTEPINIFQGNYSTDTPPIRLSYHHGNHYNSL 336
Cdd:cd22758   83 HIILQAAANLFNVRIVIIsSDGSDETTIIEPGNSKNGRTIYLGHIGENHYVSL 135

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 213 SKGFEIRRMLEDGNCLFRAVADQVYgDSEAYDLA-RQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQAL 291
Cdd:cd22753    7 SLGLYRKHIPRDGSCLFRAVSEQLF-FTQSYHQQvRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLLELEAL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334184505 292 AEMYNRPIHIYS-YSTEPINIFQGNYSTdtpPIRLSYHHGNHYNSLVD 338
Cdd:cd22753   86 SLLYKVDFIVYSiPDQPPSNITNNGYPK---KIMLCYSGGNHYDSVYS 130

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 215 GFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERD-HFSQFITEGFTSYLKRKRRDKVYGNNVEIQALAE 293
Cdd:cd22751    9 GLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPElYYEFYVPEEYDEYLKKMSKDGEWGDELTLQAAAD 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 334184505 294 MYNRPIHIY-SYSTEPINIFQgNYSTDTPP--IRLSYHHGNHYNSL 336
Cdd:cd22751   89 AFGVKIHVItSFEDNWFLEIE-PRGLVRSKrvLFLSYWAEVHYNSI 133

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 217 EIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTS---YLK--RKRRDKVYGNNVEIQAL 291
Cdd:cd22755    2 KTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESveeYLEksRMRYDGTWATDVEIFAA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334184505 292 AEMYNRPIHIYS--------YStePiNIFQGNYSTDTPPIRLSYHHGNHYN 334
Cdd:cd22755   82 ATLLGVDIYVYSkggykwllYS--P-RFKLGKRNGSREAIYLKNTNGNHFE 129

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 215 GFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEG--FTSYLKRKRRDKVYGNNVEIQALA 292
Cdd:cd22770   13 GLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDDvpFDKHVANLSKPGTYAGNDAIVAFA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 334184505 293 EMYNRPIHIYSYSTEPINIfQGNYSTDTPPIRLSYHHGNHYNS 335
Cdd:cd22770   93 RLHQVNVVIHQLNAPLWQI-RGTEKSSSRELHISYHNGDHYSS 134

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 213 SKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQALA 292
Cdd:cd22795    7 SLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQLEISALS 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 334184505 293 EMYNRPIHIYSYSTEPinifqGNYSTDT---PPIRLSYHHGNHYNSL 336
Cdd:cd22795   87 LIYNRDFILYRYPGKP-----PTYATDNgfeDKILLCCSSNGHYDSV 128

OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 203 EHQFEAEIR--YSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTS--YLKRKRR 278
Cdd:cd21880    7 EGQYVSNPRfnLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLeeYLRDAMK 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184505 279 DKVYGNNVEIQALAEMYNRPIHIYSYS-----TEPINIFQGNYSTdtppirlSY---HHGNHYNSLV 337
Cdd:cd21880   87 DGYWGGSLEAEILSKALGITIIIWVVDdsdwvTAAVRFGDGDVST-------SLnllHSGGHFDALR 146

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; Deubiquitinating enzyme OTU4, also called OTU domain-containing protein 4, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU4 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 224 DGNCLFRAVA------------DQVYGDSEAYDLaRQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQAL 291
Cdd:cd22760   10 DGRCLFRAVAhgeclargkaapDEERERELADEL-RTRAADELVKRREETEWFIEGDFDEYVARMRRPGVWGGEPELLML 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334184505 292 AEMYNRPIHIYSYSTE-----PINIFQGNYSTDTpPIRLSYHHGNHYNSLV 337
Cdd:cd22760   89 SHVLQRPITVYMADEGeggliSIAEYGQEYGKGN-PIRVLFHGFGHYEALL 138

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 216 FEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEG----FTS---YLKRKRRDKVYGNNVEI 288
Cdd:cd22757    1 FRVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSegnnYKSaeeYRADMSKPGTYGTLCEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334184505 289 QALAEMYNRPIHIYSystEPINIFQ-GNYSTDTPPIRLSYHHGN-HYNSLV 337
Cdd:cd22757   81 VAAAELYPFHFEVYR---NGKLYASfGDPSNPVKRLKFSGDLSNgHFDVLE 128

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184505 224 DGNCLFRAVADqvYGDSEAYDLaRQMCMDYMeqerdhfsqFITEGFTSYLKRKRRDKVYGNNVEIQALAEMYNRPIHIYS 303
Cdd:cd22792    8 DGNCFWHSLGH--FLGLSALEL-KKLLRDSL---------FDDPELDEELDEQLEPGVYAEDEAIAAAAKLFGVNICVHD 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334184505 304 YSTEPINIFQGNYSTDTPPIRLSyhhGNHYNSLV 337
Cdd:cd22792   76 PDEGVLYTFTPNESSKSIHLLLE---NEHFEPLV 106